2q1l

Design and Synthesis of Pyrrole-based, Hepatoselective HMG-CoA Reductase Inhibitors

Method: X-RAY DIFFRACTION

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1. Protein Identity and Related Structures Protein Identity & Related Structures

3-hydroxy-3-methylglutaryl-coenzyme A reductase

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	(3R,5R)-7-[5-(ANILINOCARBONYL)-3,4-BIS(4-FLUOROPHENYL)-1-ISOPROPYL-1H-PYRROL-2-YL]-3,5-DIHYDROXYHEPTANOIC ACID × 4 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HMDH_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 7–441； UniProt 441–875 Author chain B； PDBConstruct 7–441； UniProt 441–875 Author chain C； PDBConstruct 7–441； UniProt 441–875 Author chain D； PDBConstruct 7–441； UniProt 441–875

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2q1l
Deposition date deposition_date	2007-05-24
Structure title title	Design and Synthesis of Pyrrole-based, Hepatoselective HMG-CoA Reductase Inhibitors
Keywords keywords	OXIDOREDUCTASE, CHOLESTEROL BIOSYNTHESIS, HMG-COA, NADPH, STATIN; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2q1l__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2q1l__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2q1l__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	34.00 Å
Rg (electron density)	33.61 Å
Total Rg	34.05 Å
Atom count	12057
Residues	1603
Excluded volume	215420 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2q1l__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	3-hydroxy-3-methylglutaryl-coenzyme A reductase
Molecular weight formula_weight	47479.6 kDa
EC 编号 ec_number	1.1.1.34
Mutation mutation	M485I
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	12542

HHHHHHEPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKIN

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	(3R,5R)-7-[5-(ANILINOCARBONYL)-3,4-BIS(4-FLUOROPHENYL)-1-ISOPROPYL-1H-PYRROL-2-YL]-3,5-DIHYDROXYHEPTANOIC ACID
Molecular weight formula_weight	576.6 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	485

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6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	2q1lA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3270 — HMGR, N-terminal domain
Homologous superfamily homologous superfamily	10 — HMGR, N-terminal domain

Domain ID domain_id	2q1lA02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	770 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2

Domain ID domain_id	2q1lA03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	420 — Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain

Domain ID domain_id	2q1lB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3270 — HMGR, N-terminal domain
Homologous superfamily homologous superfamily	10 — HMGR, N-terminal domain

Domain ID domain_id	2q1lB02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	770 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2

Domain ID domain_id	2q1lB03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	420 — Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain

Domain ID domain_id	2q1lC01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3270 — HMGR, N-terminal domain
Homologous superfamily homologous superfamily	10 — HMGR, N-terminal domain

Domain ID domain_id	2q1lC02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	770 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2

Domain ID domain_id	2q1lC03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	420 — Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain

Domain ID domain_id	2q1lD01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3270 — HMGR, N-terminal domain
Homologous superfamily homologous superfamily	10 — HMGR, N-terminal domain

Domain ID domain_id	2q1lD02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	770 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2

Domain ID domain_id	2q1lD03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	420 — Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain

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Unit-cell length a length_a	74.732 Å
Unit-cell length b length_b	176.958 Å
Unit-cell length c length_c	76.735 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	118.83 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.050 Å
Low-resolution limit resolution_low	29.490 Å
R factor r_factor	0.2250
R_work r_work	0.2230
R_free r_free	0.2630

Design and Synthesis of Pyrrole-based, Hepatoselective HMG-CoA Reductase Inhibitors

1. Protein Identity and Related Structures Protein Identity & Related Structures

3-hydroxy-3-methylglutaryl-coenzyme A reductase

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2q1l__assembly_1__model_1

2q1l__assembly_1__model_1 | I(q)

2q1l__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)

Design and Synthesis of Pyrrole-based, Hepatoselective HMG-CoA Reductase Inhibitors

1. Protein Identity and Related Structures Protein Identity & Related Structures

3-hydroxy-3-methylglutaryl-coenzyme A reductase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2q1l__assembly_1__model_1

2q1l__assembly_1__model_1 | I(q)

2q1l__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)